N-glycosylation pattern of recombinant human CD82 (KAI1), a tumor-associated membrane protein

Wang, Hong; Zhang, Wei; Zhao, Jian; Zhang, Lei; Liu, Mingqi; Yan, Guoquan; Yao, Jun; Yu, Hongxiu; Yang, Pengyuan

doi:10.1016/j.jprot.2011.11.013

Cited by 23 publications

(14 citation statements)

References 38 publications

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“…The N-glycosylation pattern of CD82 was recently identified using proteomics and glycomics, determining that there are three putative N-glycosylation sites (Wang H. et al, 2012). Previously, these sites were suggested to regulate apoptosis, however the researchers did not examine the signaling that led to these apoptotic changes (Ono et al, 1999).…”

Section: Tetraspanin Post-translational Modifications and Signalingmentioning

confidence: 99%

Tetraspanins Function as Regulators of Cellular Signaling

Termini

Gillette

2017

Front. Cell Dev. Biol.

216

186

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Tetraspanins are molecular scaffolds that distribute proteins into highly organized microdomains consisting of adhesion, signaling, and adaptor proteins. Many reports have identified interactions between tetraspanins and signaling molecules, finding unique downstream cellular consequences. In this review, we will explore these interactions as well as the specific cellular responses to signal activation, focusing on tetraspanin regulation of adhesion-mediated (integrins/FAK), receptor-mediated (EGFR, TNF-α, c-Met, c-Kit), and intracellular signaling (PKC, PI4K, β-catenin). Additionally, we will summarize our current understanding for how tetraspanin post-translational modifications (palmitoylation, N-linked glycosylation, and ubiquitination) can regulate signal propagation. Many of the studies outlined in this review suggest that tetraspanins offer a potential therapeutic target to modulate aberrant signal transduction pathways that directly impact a host of cellular behaviors and disease states.

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Section: Tetraspanin Post-translational Modifications and Signalingmentioning

confidence: 99%

Tetraspanins Function as Regulators of Cellular Signaling

Termini

Gillette

2017

Front. Cell Dev. Biol.

216

186

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“…The variable region of CD82 LEL contains six cysteine residues that form three disulfide bonds and three asparagine residues for N glycosylation, which are crucial for the correct folding and motility-inhibitory activity of CD82, respectively [5]. The N-linked glycans are highly heterogeneous with distinct carbohydrate epitopes, including bisecting N-acetylglucosamine, (α-2,6) N-acetylneuraminic acid, and core fucose [13]. The transmembrane domains contain three highly conserved polar residues and interact with each other and with transmembrane domains of other tetraspanins [14].…”

Section: Cd82 Gene and Cd82 Proteinmentioning

confidence: 99%

Tetraspanin CD82: a suppressor of solid tumors and a modulator of membrane heterogeneity

Feng

Huang

Wren

et al. 2015

Cancer Metastasis Rev

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Tetraspanin CD82 suppresses the progression and metastasis of a wide range of solid malignant tumors. However, its roles in tumorigenesis and hematopoietic malignancy remain unclear. Ubiquitously expressed CD82 restrains cell migration and cell invasion by modulating both cell-matrix and cell-cell adhesiveness and confining outside-in pro-motility signaling. This restraint at least contributes to, if not determines, the metastasis-suppressive activity and, also likely, the physiological functions of CD82. As a modulator of cell membrane heterogeneity, CD82 alters microdomains, trafficking, and topography of the membrane by changing the membrane molecular landscape. The functional activities of membrane molecules and the cytoskeletal interaction of the cell membrane are subsequently altered, followed by changes in cellular functions. Given its pathological and physiological importance, CD82 is a promising candidate for clinically predicting and blocking tumor progression and metastasis and also an emerging model protein for mechanistically understanding cell membrane organization and heterogeneity.

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“…The upregulated KAI1 observed by immunofluorescent staining appears to be KAI1-s, because forskolin decreased KAI1-l. Although we do not know the mechanism responsible for the posttranslational modification of KAI1, KAI1-l might be produced post-translationally, as suggested by the recent finding that KAI1 has three N-glycosylation sites, and exhibits a highly heterogeneous N-linked glycan pattern (20). Therefore, the two different isotypes of KAI1 expressed during trophoblastic differentiation may result from posttranslational changes, like glycosylation, in BeWo cells.…”

Section: Discussionmentioning

confidence: 94%

Differential expression of the metastasis suppressor KAI1 in decidual cells and trophoblast giant cells at the feto-maternal interface

Koo¹,

Han

Yamashita³

et al. 2013

BMB Reports

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Invasion of trophoblasts into maternal uterine tissue is essential for establishing mature feto-maternal circulation. The trophoblast invasion associated with placentation is similar to tumor invasion. In this study, we investigated the role of KAI1, an anti-metastasis factor, at the maternal-fetal interface during placentation. Mouse embryos were obtained from gestational days 5.5 (E5.5) to E13.5. Immunohistochemical analysis revealed that KAI1 was expressed on decidual cells around the track made when a fertilized ovum invaded the endometrium, at days E5.5 and E7.5, and on trophoblast giant cells, along the central maternal artery of the placenta at E9.5. KAI1 in trophoblast giant cells was increased at E11.5, and then decreased at E13.5. Furthermore, KAI1 was upregulated during the forskolinmediated trophoblastic differentiation of BeWo cells. Collectively, these results indicate that KAI1 is differentially expressed in decidual cells and trophoblasts at the maternal-fetal interface, suggesting that KAI1 prevents trophoblast invasion during placentation. [BMB Reports 2013; 46(10): 507-512]

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N-glycosylation pattern of recombinant human CD82 (KAI1), a tumor-associated membrane protein

Cited by 23 publications

References 38 publications

Tetraspanins Function as Regulators of Cellular Signaling

Tetraspanins Function as Regulators of Cellular Signaling

Tetraspanin CD82: a suppressor of solid tumors and a modulator of membrane heterogeneity

Differential expression of the metastasis suppressor KAI1 in decidual cells and trophoblast giant cells at the feto-maternal interface

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